Product Spotlight for 12/3/19: A Plenitude of Proteins

This list of items represents the largest group of recombinant proteins added to our catalog since we initially included the entire category a few years ago.  We hope you find some things of interest for your research here or on the website.

Note: All the descriptions for these items come directly from the ProSpec website and have been lightly edited only for clarity and unity. Every item (except those prohibited by export restrictions) appearing on their website are also available through Peptides International.

Adiponectin is an adipocyte-specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia. The gene symbol is ADIPOQ [adiponectin, C1q and collagen domain containing]. Another designation is ACDC [adiponectin, C1q and collagen domain containing].

The protein is identical with apM1 (adipose Most abundant gene transcript-1), isolated by Maeda, et al (1996) from an adipose tissue cDNA, and GBP-28 (gelatin-binding protein of 28 kDa) (Nakano, et al, 1996), the gene of which was isolated by Saito, et al (1999), who identified the protein as the one encoded by apM1.

Human adiponectin and murine adipocyte complement related protein of 30 kDa (Acrp30; also termed adipocyte-specific secretory protein) is secreted by 3T3-L1 cells in the course of their differentiation into adipocytes are homologous proteins. The protein possesses significant homology to collagens VIII, X and complement factor C1q and has been described also as adipoQ. Wong, et al (2004) have described a widely expressed and highly conserved family of seven adiponectin paralogs that can cause increased glycogen accumulation and fatty acid oxidation and/or lower blood glucose levels in ob/ob mice (see: CTRP1, CTRP2, CTRP9).

Adiponectin is a secreted protein of 244 amino acids that belongs to a protein family possessing a collagen-like domain through which they form homo-trimers, which further combine to make oligomeric complexes (Tsao, et al, 2002). The human Adiponectin gene spans 17 kb on chromosome 3q27 (Saito, et al, 1999), consisting of three exons and two introns. Adiponectin mRNA is found in adipose tissue but not in muscle, brain, heart, intestine, kidney, liver, lung, ovary, placenta, or uterus tissues.

Schaffler, et al (1999) have shown that the Adiponectin gene is expressed by differentiated adipocytes. High levels of the protein are found in human plasma (approximately 2.0 to 17 micrograms/mL in plasma) (Hotta, et al, 2000). Adiponectin is a hormone that plays a role in the regulation of glucose and lipid homeostasis (see also: adipokines) (Tsao, et al, 2002; Berg, et al, 2002).

Ouchi, et al (1999) have determined that adiponectin suppresses TNF induced adhesion of monocytes to aortic endothelial cells and also suppresses the expression of vascular cell adhesion molecule 1 (VCAM-1), selectin E, and intercellular adhesion molecule 1 (ICAM-1 (CD54)) in these cells. Adiponectin may thus attenuate inflammation associated with atherogenesis.

Adiponectin specifically binds to collagen type 1, collagen type 3 and collagen type 5, which are present in vascular intima. As shown by Okamoto, et al (2000), the protein is detected in the walls of the catheter-injured vessels, but not in the intact vascular walls.

Levels of Adiponectin are decreased in obesity (Arita, et al, 1999; Ouchi, et al, 2003) and are reduced also in patients with coronary artery disease (Ouchi, et al, 2003).

TNF-alpha reduces the expression and secretion of apM1 in differentiating primary human pre-adipocytes (Kappes and Loffler, 2000). Adiponectin inhibits the expression of endothelial adhesion molecules induced by TNF-alpha through a mechanism involving the suppression of TNF-alpha induced I-kappa-B-alpha phosphorylation and subsequent NF-kappa-B activation that does not affect other signals mediated by TNF-alpha (Ouchi, et al, 2000. Adiponectin has an inhibitory effect on proliferation of vascular smooth muscle cells. Arita, et al (2002) have reported that Adiponectin suppresses proliferation and migration of human aortic smooth muscle cells stimulated with PDGF-BB (but not HB-EGF or PDGF-AA), by acting as a plasma binding protein for PDGF-BB. Adiponectin also strongly and dose-dependently suppresses phosphorylation of p42/44 extracellular signal-related kinase (ERK) phosphorylation induced by PDGF-BB, PDGF-AA, and HB-EGF.

As shown by Yokota, et al (2000), adiponectin also suppresses functions of mature macrophages, inhibiting their phagocytic activity and their production of TNF-alpha induced by bacterial lipopolysaccharides. Ouchi, et al (2001) have shown that adiponectin suppresses lipid accumulation and class A scavenger receptor expression in human macrophages derived from monocytes. Yokota, et al (2000) reveal Adiponectin to be an important negative regulator in hematopoiesis and the immune system. Adiponectin predominantly inhibits proliferation of myelomonocytic lineage cells (see also: hematopoiesis). Some of the effects may be due to apoptosis. Kobayashi, et al (2004) have reported that a high molecular weight form of adiponectin suppresses apoptosis and caspase-3 activity in human umbelical vein endothelial cells.

Adiponectin suppresses colony formation from the hematopoietic progenitor cells CFU-GM, CFU-G, and CFU-M but does not affect BFU-E or mixed erythroid-myeloid CFU (Yokota, et al, 2000). Adiponectin also inhibits proliferation of several myeloid cell lines (4/9 studied) but has no effects on erythroid or lymphoid cell lines except for one cell line.

DiMascio, et al (2007) have investigated the role of adiponectin in hematopoietic stem cell function and shown that adiponectin is expressed by adipocytes in the bone marrow and that adiponectin receptors are expressed by hematopoietic stem cells. Adiponectin increases the proliferation of hematopoietic stem cells and retains them in a functionally immature state. Adiponectin signaling is required for optimal proliferation of hematopoietic stem cells in vitro and in long term hemopoietic reconstitution in vivo (see also: LTRC [long-term repopulating cells].  Yamauchi, et al (2004) have cloned the cDNAs for two adiponectin receptors, both of which bind full-length adiponectin and globular adiponectin and mediate antidiabetic metabolic effects. T-cadherin has been identified as a receptor for hexameric and high molecular weight forms of adiponectin and may act as a co-receptor (Hug, et al, 2004). Maeda, et al (2002) have studied transgenic knock-out mice lacking expression of adiponectin. Clearance of free fatty acid in plasma in these mice is delayed. The animals also low levels of fatty acid transport protein 1 (FATP-1) mRNA in muscle, high levels of TNF-alpha mRNA in adipose tissue, high plasma TNF-alpha concentrations, and impaired insulin signaling, all of which contribute to the severe diet-induced insulin resistance observed.

We are pleased to offer fourteen new versions of adiponectin for your research needs.

Acrp30 Protein

Acrp30 Human, HEK

Acrp30 (108-244) Human

Acrp30 Human

Acrp30 Human, HMW

Acrp30 Human, Sf9

Acrp30 Human, Trimeric

Acrp30 Mouse, HEK

Acrp30 Mouse, His

Acrp30 Mouse, Trimeric

gAcrp30 Human, His

gAcrp30 Mouse

Acrp30 Human, His

Acrp30 Human, HMW

The binding of lipids and cholesterol to Apoliproteins result in the formation of lipoproteins which carry lipids through the circulatory and lymphatic organs. Apo A1 is the major protein component of high-density lipoprotein (HDL).[1] Deficiency of APOA1 is related with HDL deficiencies and is involved in protection against Alzheimer. APOA and APOAE cooperate to adjust the levels of triglyceride in coronary heart disease.

6 main classes of apolipoproteins are APOA, APOB, APOC, APOD, APOE and APOH. APOA1 takes an important role in the return of surplus cholesterol from peripheral tissues to the liver. Lipoprotein lipid molecules are precipitate in water thus being insoluble. Nevertheless, due to of their amphipathic/detergent like characteristics, Apolipoproteins fence in the lipids, forming a lipoprotein particle which is soluble in water, hence travel in blood. The successful transport of dietary and endogenous lipids to peripheral tissues which are used as an energy source is due to APOB and APOE Apolipoprtoeins. APOE is primarily located in HDL and VLDL Apolipoproteins act as lipid transfer carrier enzymes, cofactors and receptor ligands which control lipoprotein metabolism.

Apolipoproteins are composed from various lipoproteins such as exchangeable Apolipoprtoeins and non-exchangeable. An example of non-exchangeable apolipoprotein is APOAB which is attached to the lipoprotein particle while examples of Lipoprotein exchangeable are APOM, APOD, APOJ, APOH and APOA1 which are transported between different lipoprotein molecules. APOB and APOA1 are the main protein components of LDL and HDL. APOB can be found in 2 formations, 2% APOB-48 and 98% APOB-100. APOB-48 is formed in the intestine and APOB-100 is formed in the liver, fused to LDL and regulates ligand–receptor uptake of LDL to circulate in its free form.

APOA5 Human, HEK

Erythropoietin is commonly referred to as hematopoietin or hemopoietin. It is also known in its abbreviated form of EPO. This is a glycoprotein cytokine that’s primarily secreted by the kidney. This secretion takes place as the result of cellular hypoxia. This is a condition in which a part of the body doesn’t receive as much oxygen as it needs. The most common causes of hypoxia in cells is anemia. As a result, people suffering from anemia are found to have increased levels of EPO. The consequence of EPO secretion is the stimulation of red blood cell production in bone marrow. Everybody constantly has a low level of EPO secreted throughout their body, to act as compensation for regular red blood cell turnover.

The primary function of erythropoietin is to produce more red blood cells. If bodies lack EPO, then the process in which red blood cells are produced cannot take place. The kidney produces EPO when hypoxic conditions are present in cells. EPO is found to have most of its effect in the bone marrow of humans, as this is where red blood cell precursors and progenitors are found. It works to protect these cells from death.

Aside from the function of EPO on red blood cell production, there are other functions linked to it. These include stimulating angiogenesis (the process in which new blood vessels are created from pre-existing ones), vasoconstriction-dependent hypertension, and improving cell survival through activating EPO receptors.

EPO has received a lot of attention in the modern world of athletics as performance-based athletes have attempted to manufacturer an increase in EPO production within their cells. This would boost the oxygen levels in their blood, thereby increasing red blood cell production and helping with endurance.

Erythropoietin completes its functions by binding to its receptor, EpoR. EPO must bind with EpoR while on the red blood cell progenitor surface. In doing so, this leads to the activation of a JAK2 signaling avalanche. Following this, the STAT5, PIK3 and Ras MAPK pathways are initiated too. The consequence of this is differentiation, as well as the survival and multiplication of the erythroid cell. Increased levels of EpoR expression are often confined to the erythroid progenitor cells.

EPO is produced by fibroblasts present in the kidney. These fibroblasts are closely linked with the peritubular capillary and proximal convoluted tubule. EPO can also be found in the perisinusoidal cells within the liver. It is found that liver production mainly occurs in pregnant women during the perinatal period. On the contrary, production via the kidneys is the most common production found in all humans during adulthood.

Levels of EPO in the blood are naturally very low, unless anemia is present. It is thought that the production of EPO can multiply by 1000 when cells are suffering from anemia.

EPO is a glycoprotein weight approximately 30,400 daltons. 165 amino acids are being produced by this protein; primarily via the kidneys and liver. It will bind on a certain membrane receptor, which in turn activates multiple signaling pathways.

EPO, Clone PAT1C12AT

EPO a Human, Sf9

EPOR Human, Active

Following closely at the conclusion of National Breast Cancer Awareness Month, which takes place in October annually, we have two items of interest related to that research.

BRMS1 protein, a member of the mSin3a family of HDAC (histone deacetylase complexes), is mainly restricted to the nucleus. BRMS1 holds two coiled-coil motifs and a few imperfect leucine zipper motifs. BRMS1 reduces the metastatic potential, but not the tumorogenicity, of melanoma cell lines and human breast cancer. Alternative splicing creates two transcript variants encoding different isoforms.

Breast Cancer Metastasis Suppressor 1 Human Recombinant

Breast Cancer Anti-Estrogen Resistance 1 (BCAR1) is a Src family kinase substrate which takes part in a range of cellular events such as migration, survival, transformation, and invasion. BCAR1 plays a vital role for tyrosine kinase-based signaling related to cell adhesion.

Breast Cancer Anti-Estrogen Resistance 1 Human Recombinant

FK506 Binding Protein is related to the cyclophilins in terms of function, although they do not share the same amino acid sequence. Sometimes referred to as FKBP, FK506 binding protein is a member of the immunophilin family and has been shown to exist in various eukaryotes.

FKBP refers to a number of different binding proteins, which may have different mechanisms of action. However, the FK506 binding protein has been shown to act as molecular switches by binding directly to their target proteins and altering their shape and structure. For example, the FKBP12-FK506 complex is created when FK506 binds to cytosolic FKBP12.

FK506 binding proteins have a number of functions, some of which are still emerging. Within the FK506 binding proteins family, FKBP12 is known to bind with immunosuppressant drugs, Rapamycin, and Tacrolimus (also known as FK506). Operating as a cis/trans peptidyl prolyl isomerase (PPIase), FKBP12 then begins the process of interconversion between prolyl cis/trans conformations.With a range of functions, FKBPs are involved in protein folding, apoptosis, cellular functioning, and transcription. Due to their varied functions, studies have suggested that FKBPs may be involved with the regulation of cardiac function, immunosuppression, neurodegenerative diseases, cancer, neuronal development, and function, as well as heart disease.

With the FK506 binding proteins family, FKBP12 is expressed in all types of tissues and has been identified as a 12 kDa cytosolic protein. FKBP38 contains 413 amino acids and has a predicted size of 45 kDa, however, there have been some discrepancies over the exact structure of FKBP38 in the past. Residing in both the nucleus and cytoplasm, FKBP52 is a co-chaperone of heat-shock protein 90 (Hsp90) and has an active role in steroid receptor regulation. Sharing 60% of sequencing homology with FKBP52, FKBP51 also features Ca2+/CaM binding motif, three TPR domains and two PPIase domains.

In contrast, FKBP36 lacks PPIase activity but contains a C-terminal TPR domain and an N-terminal PPIase domain. Whilst FKBP36 lacks PPIase activity, it remains able to bind with various proteins due to its TPR and PPIase domains. FKBP57 also contains a TPR domain at its C-terminus, as well as a PPIase domain at its N-terminus. Defined as an aryl hydrocarbon receptor-interacting protein, FKBP57 doesn’t exhibit PPIase activity, nor does it bind to FK506. However, its structure does enable it to interact with Hsp90 via its TPR and PPIase domains.
In addition to this, FKBPP25 features a nuclear targeting sequence and includes a PPIase domain at its C-terminus and a hydrophilic helix-loop-helix (HLH) motif at its N-terminus. Finally, FKBP133, sometimes known as WAFL, is comprised of a PPIase domain and a Wiskott-Aldrich syndrome protein homology region1(WH1).

TPR domains are commonly involved in mediating protein-protein interactions, which means many of the proteins within the FK506 family work in this way. In relation to immunosuppression, the FK506-FKBP12 complex interacts with calcineurin (CaN), which is a Ca2+-dependent serine-threonine phosphatase. When present in muscle cells, FKBP12 has been shown to interact with the Ca2+ release channels of the sarcoplasmic reticulum (SR) ryanodine receptors (RyRs), whilst FKBP57 interacts with hsp90 via both PPIase and TPR domains.

FKBP5 Human

FKBP6 Antibody

Finally, for brevity’s sake, the final six individual entries are just listed below without introductions, since this is already by far the longest Product Spotlight to date!  However, you can click through their respective links for more information.

C1QTNF3 Human

MCP 1 Rat

ProInsulin C-Peptide Analogue Human Recombinant

Glutaredoxin Mouse Recombinant

Programmed Cell Death 4, His Tag Human Recombinant


For any information about these or our thousands of other recombinant protein offerings – or other peptide or related products - please contact us via email through this link.